ArticlePloS one2010
In silico identification of carboxylate clamp type tetratricopeptide repeat proteins in Arabidopsis and rice as putative co-chaperones of Hsp90/Hsp70.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 92 citations in OpenAlex.
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- Enrichment of intrinsically disordered residues in ohnologs facilitates abiotic stress resilience in Brassica rapa.Journal of plant research · 2023Article
- A myosin XI adaptor, TAPE, is essential for pollen tube elongation in rice.Plant physiology · 2022Article
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- Beyond the Usual Suspects: Physiological Roles of the Arabidopsis Amidase Signature (AS) Superfamily Members in Plant Growth Processes and Stress Responses.Biomolecules · 2021Review
- Gene co-expression network analysis of the heat-responsive core transcriptome identifies hub genes in Brassica rapa.Planta · 2021Article
- Luminescence complementation assay for measurement of binding to protein C-termini in live cells.Analytical biochemistry · 2020Article
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- HOP, a Co-chaperone Involved in Response to Stress in Plants.Frontiers in plant science · 2020Review
- Host protein chaperones, RNA helicases and the ubiquitin network highlight the arms race for resources between tombusviruses and their hosts.Advances in virus research · 2020Article
- Heat Shock Proteins: Dynamic Biomolecules to Counter Plant Biotic and Abiotic Stresses.International journal of molecular sciences · 2019Review
- Genome-wide analysis of the rice J-protein family: identification, genomic organization, and expression profiles under multiple stresses.3 Biotech · 2019Review
- Construction of restorer lines and molecular mapping for restorer gene of hau cytoplasmic male sterility in Brassica napus.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2019Article
- TTL Proteins Scaffold Brassinosteroid Signaling Components at the Plasma Membrane to Optimize Signal Transduction in Arabidopsis.The Plant cell · 2019Article
- Time-resolved interaction proteomics of the GIGANTEA protein under diurnal cycles in Arabidopsis.FEBS letters · 2019Article
- Dissecting genomic hotspots underlying seed protein, oil, and sucrose content in an interspecific mapping population of soybean using high-density linkage mapping.Plant biotechnology journal · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The essential eukaryotic molecular chaperone Hsp90 operates with the help of different co-chaperones, which regulate its ATPase activity and serve as adaptors to recruit client proteins and other molecular chaperones, such as Hsp70, to the Hsp90 complex. Several Hsp90 and Hsp70 co-chaperones contain the tetratricopeptide repeat (TPR) domain, which interacts with the highly conserved EEVD motif at the C-terminal ends of Hsp90 and Hsp70. The acidic side chains in EEVD interact with a subset of basic residues in the TPR binding pocket called a 'carboxylate clamp'. Since the carboxylate clamp residues are conserved in the TPR domains of known Hsp90/Hsp70 co-chaperones, we carried out an in silico search for TPR proteins in Arabidopsis and rice comprising of at least one three-motif TPR domain with conserved amino acid residues required for Hsp90/Hsp70 binding. This approach identified in Arabidopsis a total of 36 carboxylate clamp (CC)-TPR proteins, including 24 novel proteins, with potential to interact with Hsp90/Hsp70. The newly identified CC-TPR proteins in Arabidopsis and rice contain additional protein domains such as ankyrin, SET, octicosapeptide/Phox/Bem1p (Phox/PB1), DnaJ-like, thioredoxin, FBD and F-box, and protein kinase and U-box, indicating varied functions for these proteins. To provide proof-of-concept of the newly identified CC-TPR proteins for interaction with Hsp90, we demonstrated interaction of AtTPR1 and AtTPR2 with AtHsp90 in yeast two-hybrid and in vitro pull down assays. These findings indicate that the in silico approach used here successfully identified in a genome-wide context CC-TPR proteins with potential to interact with Hsp90/Hsp70, and further suggest that the Hsp90/Hsp70 system relies on TPR co-chaperones more than it was previously realized.
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